Anti-BiP/GRP78 (C-terminus)
产品名称: Anti-BiP/GRP78 (C-terminus)
英文名称:
产品编号: 200310-9E4
产品价格: null
产品产地: 成都正能生物
品牌商标: 正能抗体
更新时间: null
使用范围: WB
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Size 100ul
Cat code 200310-9E4
Species Cross-reactivity H,R
Key Application WB
Host Mouse
Clone Number 9E4-2A7-H6
Antibody type Monoclonal antibody
Purified method Affinity purified
Isotype IgG1
Molecular Weight 78kDa
Sensitivity This antibody detects endogenous levels of BiP/GRP78 and does not cross-react with related proteins.
Immunogen Purified recombinant human BiP/GRP78 protein fragments expressed in E.coli.
UniProt Number P11021
GeneBank ID NM_005347
Subcellular location Endoplasmic reticulum lumen. Melanosome
Formulation Purified mouse monoclonal in PBS(pH 7.4) containing with 0.02% sodium azide and 50% glycerol.
Altername MIF2;HSPA5;FLJ26106
Gene_symbol BIP; MIF2; GRP78
Summary The 78 kDa glucose regulated protein/BiP (GRP78) belongs to the family of ~70 kDa heat shock proteins (HSP 70). GRP78 is a resident protein of the endoplasmic reticulum (ER) and may associate transiently with a variety of newly synthesized secretory and membrane proteins or permanently with mutant or defective proteins that are incorrectly folded, thus preventing their export from the ER lumen. GRP78 is a highly conserved protein that is essential for cell viability. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the C terminus of GRP78 and other resident ER proteins including glucose regulated protein 94 (GRP 94) and protein disulfide isomerase (PDI). The presence of carboxy terminal KDEL appears to be necessary for retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.
UniPort summary Function Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER
Application Images :
Western blot detection of HSPA5 antibody in Hela,C6,Lncap and MDA-MB-468 cell lysates using HSPA5 antibody (1:1000 diluted).Predicted band size:72KDa.Observed band size:78KDa.